High yield expression and NMR characterization of Arkadia E3 ubiquitin ligase RING-H2 finger domain
Copyright policy )High yield expression and NMR characterization of Arkadia E3 ubiquitin ligase RING-H2 finger domain
E3 ubiquitin ligases play a key role in the recognition of target proteins and the degradation by 26S proteasomes. Arkadia is the first example of an E3 ubiquitin ligase that positively regulates TGF-beta family signaling. It has been shown to induce ubiquitin-dependent degradation of negative regulators of TGF-beta signaling through its C-terminal RING domain. Structural analysis of Arkadia RING domain is needed to elucidate its enzymatic properties. For such studies efficient production of pure and correctly folded Arkadia protein is required. Here we report the recombinant expression in Escherichia coli and purification of the C-terminal RING domain of Arkadia. NMR analysis of the soluble construct reveals a stable folded protein suitable for high resolution structural studies.
- University of Freiburg Germany
- Imperial College Healthcare NHS Trust United Kingdom
- Drittes Physikalisches Institut Germany
- Imperial College London United Kingdom
- University of Patras Greece
Protein Folding, Ubiquitin, Ubiquitin-Protein Ligases, Molecular Sequence Data, Recombinant Proteins, Transforming Growth Factor beta1, Mice, Zinc, Escherichia coli, Animals, Amino Acid Sequence, RING Finger Domains, Nuclear Magnetic Resonance, Biomolecular
Protein Folding, Ubiquitin, Ubiquitin-Protein Ligases, Molecular Sequence Data, Recombinant Proteins, Transforming Growth Factor beta1, Mice, Zinc, Escherichia coli, Animals, Amino Acid Sequence, RING Finger Domains, Nuclear Magnetic Resonance, Biomolecular
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